The role of cyclic nucleotide-independent phosphorylation reactions in the hormonal control of cell metabolism, proliferation and differentiation will be examined. Three cyclic nucleotide-independent protein kinases from reticulocytes, previously obtained in a highly purified form, will be examined in detail. In addition, three other cyclic nucleotide-independent protein kinases which have been indentified and partially purified from reticulocytes will be prepared in a highly purified form and characterized. The two major forms of phosphoprotein phosphatase from reticulocytes will also be purified further and the physico/chemical properties of the enzymes will be completed. The mode(s) of regulation of the protein kinases and phosphoprotein phosphatases will be identified. Antibody to the purified enzymes will be prepared and used to quantitate the levels of the various enzymes under conditions of hormonal stimulation. Several cell types which are insulin sensitive will be examined and the protein kinase and phosphoprotein phosphatase activities will be correlated with alterations in the phosphorylation patterns.